HEADER ISOMERASE 12-MAR-10 3M5P
TITLE GLUCOSE-6-PHOSPHATE ISOMERASE FROM FRANCISELLA TULARENSIS COMPLEXED
TITLE 2 WITH FRUCTOSE-6-PHOSPHATE.
CAVEAT 3M5P F6P A 701 HAS WRONG CHIRALITY AT ATOM C2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSE-6-PHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GPI, PHOSPHOGLUCOSE ISOMERASE, PGI, PHOSPHOHEXOSE ISOMERASE,
COMPND 5 PHI;
COMPND 6 EC: 5.3.1.9;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FRANCISELLA TULARENSIS SUBSP. TULARENSIS;
SOURCE 3 ORGANISM_TAXID: 119856;
SOURCE 4 STRAIN: SCHU S4;
SOURCE 5 GENE: FTT1315C, PGI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, IDP02733, GLUCOSE-6-PHOSPHATE, ISOMERASE,
KEYWDS 2 FRUCTOSE-6-PHOSPHATE., CYTOPLASM, GLUCONEOGENESIS, GLYCOLYSIS,
KEYWDS 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,N.MALTSEVA,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 4 06-OCT-21 3M5P 1 REMARK SEQADV HETSYN
REVDAT 3 29-JUL-20 3M5P 1 CAVEAT COMPND REMARK SEQADV
REVDAT 3 2 1 HETNAM LINK SITE
REVDAT 2 08-NOV-17 3M5P 1 REMARK
REVDAT 1 23-MAR-10 3M5P 0
JRNL AUTH J.OSIPIUK,N.MALTSEVA,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK
JRNL TITL X-RAY CRYSTAL STRUCTURE OF GLUCOSE-6-PHOSPHATE ISOMERASE
JRNL TITL 2 FROM FRANCISELLA TULARENSIS COMPLEXED WITH
JRNL TITL 3 FRUCTOSE-6-PHOSPHATE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 75874
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.132
REMARK 3 R VALUE (WORKING SET) : 0.131
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3810
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5163
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 290
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4322
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 503
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.69000
REMARK 3 B22 (A**2) : -0.69000
REMARK 3 B33 (A**2) : 1.04000
REMARK 3 B12 (A**2) : -0.35000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.099
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.971
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.976
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4796 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3257 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6553 ; 1.453 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8075 ; 0.937 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 636 ; 5.444 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 240 ;37.268 ;25.750
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 915 ;14.270 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;17.655 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 720 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5389 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 922 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2848 ; 1.311 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1157 ; 0.435 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4643 ; 2.041 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1948 ; 3.440 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1857 ; 5.088 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 8053 ; 1.417 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -10 A 9999
REMARK 3 ORIGIN FOR THE GROUP (A): 46.9613 57.0017 2.5998
REMARK 3 T TENSOR
REMARK 3 T11: 0.0115 T22: 0.0457
REMARK 3 T33: 0.0196 T12: -0.0182
REMARK 3 T13: -0.0079 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.9250 L22: 0.6797
REMARK 3 L33: 0.6442 L12: -0.3166
REMARK 3 L13: 0.3825 L23: -0.2677
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: 0.0109 S13: 0.0276
REMARK 3 S21: 0.0197 S22: -0.0571 S23: -0.1044
REMARK 3 S31: -0.0268 S32: 0.1226 S33: 0.0485
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3M5P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058140.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76000
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 32.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.68
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.66400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.140
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, SOLVE, RESOLVE, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM/POTASSIUM PHOSPHATE
REMARK 280 BUFFER, 35% MPD, 10 MM FRUCTOSE-6-PHOSPHATE, PH 6.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.81533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.90767
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.90767
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 55.81533
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: BIOLOGICAL UNIT IS A DIMER.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 524 CA CB CG CD OE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 796 O HOH A 831 2.15
REMARK 500 OD2 ASP A 256 O HOH A 925 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 37 -122.00 53.97
REMARK 500 ASP A 149 -54.92 -138.55
REMARK 500 CYS A 164 11.58 -155.92
REMARK 500 SER A 173 -67.19 -147.18
REMARK 500 THR A 363 -127.83 -109.05
REMARK 500 ALA A 378 -61.35 -126.60
REMARK 500 SER A 400 -157.83 -103.86
REMARK 500 GLN A 498 63.78 -158.87
REMARK 500 ASP A 517 96.37 -160.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 704 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 61 O
REMARK 620 2 SER A 63 O 92.2
REMARK 620 3 HOH A 637 O 81.4 167.1
REMARK 620 4 HOH A 671 O 77.3 77.5 90.1
REMARK 620 5 HOH A 751 O 167.1 82.5 101.3 90.1
REMARK 620 6 HOH A1034 O 88.0 97.5 93.5 164.1 104.4
REMARK 620 N 1 2 3 4 5
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LJK RELATED DB: PDB
REMARK 900 GLUCOSE-6-PHOSPHATE ISOMERASE FROM FRANCISELLA TULARENSIS COMPLEXED.
REMARK 900 RELATED ID: IDP02733 RELATED DB: TARGETDB
DBREF 3M5P A 1 540 UNP Q5NFC4 G6PI_FRATT 1 540
SEQADV 3M5P SER A -2 UNP Q5NFC4 EXPRESSION TAG
SEQADV 3M5P ASN A -1 UNP Q5NFC4 EXPRESSION TAG
SEQADV 3M5P ALA A 0 UNP Q5NFC4 EXPRESSION TAG
SEQADV 3M5P LEU A 194 UNP Q5NFC4 PHE 194 ENGINEERED MUTATION
SEQRES 1 A 543 SER ASN ALA MSE LEU PHE CYS ASP ASP SER LYS LYS TYR
SEQRES 2 A 543 LEU LYS GLU GLN ASN ILE ASN LEU LYS ASN GLU PHE ASP
SEQRES 3 A 543 LYS ASP ASP LYS ARG VAL GLU LYS PHE SER LEU LYS HIS
SEQRES 4 A 543 GLN ASN ILE TYR PHE ASP TYR SER LYS ASN LEU ILE ASN
SEQRES 5 A 543 ASP TYR ILE LEU LYS SER LEU LEU GLU SER ALA GLU LYS
SEQRES 6 A 543 SER SER LEU LYS ASP LYS ILE LYS GLN MSE PHE ASN GLY
SEQRES 7 A 543 ALA LYS ILE ASN SER THR GLU HIS ARG ALA VAL LEU HIS
SEQRES 8 A 543 THR ALA LEU ARG ASP LEU SER SER THR PRO LEU ILE VAL
SEQRES 9 A 543 ASP GLY GLN ASP ILE ARG GLN GLU VAL THR LYS GLU LYS
SEQRES 10 A 543 GLN ARG VAL LYS GLU LEU VAL GLU LYS VAL VAL SER GLY
SEQRES 11 A 543 ARG TRP ARG GLY PHE SER GLY LYS LYS ILE THR ASP ILE
SEQRES 12 A 543 VAL ASN ILE GLY ILE GLY GLY SER ASP LEU GLY PRO LYS
SEQRES 13 A 543 MSE VAL VAL ARG ALA LEU GLN PRO TYR HIS CYS THR ASP
SEQRES 14 A 543 LEU LYS VAL HIS PHE VAL SER ASN VAL ASP ALA ASP SER
SEQRES 15 A 543 LEU LEU GLN ALA LEU HIS VAL VAL ASP PRO GLU THR THR
SEQRES 16 A 543 LEU LEU ILE ILE ALA SER LYS SER PHE SER THR GLU GLU
SEQRES 17 A 543 THR LEU LEU ASN SER ILE SER ALA ARG GLU TRP LEU LEU
SEQRES 18 A 543 ASP HIS TYR GLU ASP GLU LYS ALA VAL ALA ASN HIS PHE
SEQRES 19 A 543 VAL ALA ILE SER SER LYS LEU ASP LYS VAL LYS GLU PHE
SEQRES 20 A 543 GLY ILE ASP LEU GLU HIS CYS TYR LYS MSE TRP ASP TRP
SEQRES 21 A 543 VAL GLY GLY ARG TYR SER LEU TRP SER SER ILE GLY MSE
SEQRES 22 A 543 SER ILE ALA PHE ALA ILE GLY TYR ASP ASN PHE GLU LYS
SEQRES 23 A 543 LEU LEU ALA GLY ALA TYR SER VAL ASP LYS HIS PHE LYS
SEQRES 24 A 543 GLU THR GLU PHE SER LYS ASN ILE PRO VAL ILE MSE ALA
SEQRES 25 A 543 LEU LEU ALA SER TYR TYR SER CYS THR TYR ASN SER GLN
SEQRES 26 A 543 SER GLN ALA LEU LEU PRO TYR ASP GLU ARG LEU CYS TYR
SEQRES 27 A 543 PHE VAL ASP TYR LEU GLN GLN ALA ASP MSE GLU SER ASN
SEQRES 28 A 543 GLY LYS SER VAL ASN ILE ALA GLY GLU THR VAL ASN TYR
SEQRES 29 A 543 GLN THR GLY VAL VAL LEU TRP GLY GLY VAL GLY THR ASN
SEQRES 30 A 543 GLY GLN HIS ALA PHE HIS GLN LEU LEU HIS GLN GLY ASN
SEQRES 31 A 543 ILE PHE ILE PRO VAL ASP PHE ILE ALA ILE ALA THR SER
SEQRES 32 A 543 HIS HIS ASN TYR ASP ASN HIS GLN GLN ALA LEU LEU ALA
SEQRES 33 A 543 ASN CYS PHE ALA GLN SER GLN ALA LEU MSE PHE GLY GLN
SEQRES 34 A 543 SER TYR ASP MSE VAL TYR ASN GLU LEU LEU LYS SER GLY
SEQRES 35 A 543 LEU ASN GLU THR GLN ALA LYS GLU LEU ALA ALA HIS LYS
SEQRES 36 A 543 VAL ILE PRO GLY ASN ARG PRO SER THR THR ILE LEU LEU
SEQRES 37 A 543 ASP GLU LEU SER PRO TYR SER LEU GLY ALA LEU ILE ALA
SEQRES 38 A 543 LEU TYR GLU HIS LYS ILE PHE VAL GLN GLY VAL LEU TRP
SEQRES 39 A 543 ASP ILE ASN SER TYR ASP GLN TRP GLY VAL GLU LEU GLY
SEQRES 40 A 543 LYS LYS LEU GLY LYS ASN ILE LEU LYS ALA MSE ASN ASP
SEQRES 41 A 543 ASP SER SER ASP GLU TYR GLN ASN LEU ASP ASP SER THR
SEQRES 42 A 543 ARG GLN LEU ILE ALA LYS VAL LYS ASN LYS
MODRES 3M5P MSE A 1 MET SELENOMETHIONINE
MODRES 3M5P MSE A 72 MET SELENOMETHIONINE
MODRES 3M5P MSE A 154 MET SELENOMETHIONINE
MODRES 3M5P MSE A 254 MET SELENOMETHIONINE
MODRES 3M5P MSE A 270 MET SELENOMETHIONINE
MODRES 3M5P MSE A 308 MET SELENOMETHIONINE
MODRES 3M5P MSE A 345 MET SELENOMETHIONINE
MODRES 3M5P MSE A 423 MET SELENOMETHIONINE
MODRES 3M5P MSE A 430 MET SELENOMETHIONINE
MODRES 3M5P MSE A 515 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 72 8
HET MSE A 154 8
HET MSE A 254 8
HET MSE A 270 8
HET MSE A 308 8
HET MSE A 345 8
HET MSE A 423 13
HET MSE A 430 13
HET MSE A 515 8
HET F6P A 701 16
HET GOL A 702 12
HET GOL A 703 6
HET NA A 704 1
HET PO4 A 705 5
HET PO4 A 706 5
HETNAM MSE SELENOMETHIONINE
HETNAM F6P 6-O-PHOSPHONO-BETA-D-FRUCTOFURANOSE
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETNAM PO4 PHOSPHATE ION
HETSYN F6P FRUCTOSE-6-PHOSPHATE; 6-O-PHOSPHONO-BETA-D-FRUCTOSE; 6-
HETSYN 2 F6P O-PHOSPHONO-D-FRUCTOSE; 6-O-PHOSPHONO-FRUCTOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 2 F6P C6 H13 O9 P
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 NA NA 1+
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 8 HOH *503(H2 O)
HELIX 1 1 ASP A 5 LYS A 12 1 8
HELIX 2 2 GLU A 13 ASN A 15 5 3
HELIX 3 3 ASN A 17 ASP A 25 1 9
HELIX 4 4 LYS A 27 PHE A 32 1 6
HELIX 5 5 ASN A 49 SER A 63 1 15
HELIX 6 6 SER A 64 GLY A 75 1 12
HELIX 7 7 LEU A 87 ARG A 92 1 6
HELIX 8 8 ILE A 106 SER A 126 1 21
HELIX 9 9 ILE A 145 SER A 148 5 4
HELIX 10 10 ASP A 149 LEU A 159 1 11
HELIX 11 11 GLN A 160 HIS A 163 5 4
HELIX 12 12 ASP A 176 HIS A 185 1 10
HELIX 13 13 VAL A 186 VAL A 187 5 2
HELIX 14 14 ASP A 188 GLU A 190 5 3
HELIX 15 15 THR A 203 GLU A 222 1 20
HELIX 16 16 ASP A 223 LYS A 225 5 3
HELIX 17 17 ALA A 226 HIS A 230 1 5
HELIX 18 18 LYS A 237 GLY A 245 1 9
HELIX 19 19 ASP A 247 GLU A 249 5 3
HELIX 20 20 GLY A 259 SER A 263 5 5
HELIX 21 21 SER A 266 ILE A 268 5 3
HELIX 22 22 GLY A 269 GLY A 277 1 9
HELIX 23 23 GLY A 277 THR A 298 1 22
HELIX 24 24 GLU A 299 LYS A 302 5 4
HELIX 25 25 ASN A 303 TYR A 319 1 17
HELIX 26 26 ASP A 330 CYS A 334 5 5
HELIX 27 27 TYR A 335 GLY A 349 1 15
HELIX 28 28 THR A 373 ALA A 378 5 6
HELIX 29 29 PHE A 379 GLY A 386 1 8
HELIX 30 30 TYR A 404 GLY A 425 1 22
HELIX 31 31 SER A 427 SER A 438 1 12
HELIX 32 32 ASN A 441 VAL A 453 1 13
HELIX 33 33 SER A 469 TRP A 491 1 23
HELIX 34 34 GLN A 498 GLY A 500 5 3
HELIX 35 35 VAL A 501 ASP A 517 1 17
HELIX 36 36 SER A 520 LEU A 526 1 7
HELIX 37 37 ASP A 527 LYS A 540 1 14
SHEET 1 A 6 SER A 33 HIS A 36 0
SHEET 2 A 6 ILE A 39 ASP A 42 -1 O PHE A 41 N LEU A 34
SHEET 3 A 6 THR A 461 LEU A 465 -1 O LEU A 464 N TYR A 40
SHEET 4 A 6 VAL A 392 ILE A 397 1 N PHE A 394 O THR A 461
SHEET 5 A 6 SER A 323 PRO A 328 1 N LEU A 327 O ASP A 393
SHEET 6 A 6 VAL A 366 GLY A 369 1 O TRP A 368 N LEU A 326
SHEET 1 B 2 ILE A 100 VAL A 101 0
SHEET 2 B 2 GLN A 104 ASP A 105 -1 O GLN A 104 N VAL A 101
SHEET 1 C 5 LYS A 168 VAL A 172 0
SHEET 2 C 5 ASP A 139 ILE A 143 1 N ASN A 142 O VAL A 172
SHEET 3 C 5 THR A 192 ALA A 197 1 O ALA A 197 N ILE A 143
SHEET 4 C 5 PHE A 231 SER A 235 1 O ILE A 234 N ILE A 196
SHEET 5 C 5 CYS A 251 LYS A 253 1 O TYR A 252 N ALA A 233
SSBOND 1 CYS A 4 CYS A 317 1555 1555 2.13
LINK C ALA A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N LEU A 2 1555 1555 1.34
LINK C GLN A 71 N MSE A 72 1555 1555 1.32
LINK C MSE A 72 N PHE A 73 1555 1555 1.34
LINK C LYS A 153 N MSE A 154 1555 1555 1.34
LINK C MSE A 154 N VAL A 155 1555 1555 1.32
LINK C LYS A 253 N MSE A 254 1555 1555 1.32
LINK C MSE A 254 N TRP A 255 1555 1555 1.31
LINK C GLY A 269 N MSE A 270 1555 1555 1.35
LINK C MSE A 270 N SER A 271 1555 1555 1.33
LINK C ILE A 307 N MSE A 308 1555 1555 1.33
LINK C MSE A 308 N ALA A 309 1555 1555 1.33
LINK C ASP A 344 N MSE A 345 1555 1555 1.33
LINK C MSE A 345 N GLU A 346 1555 1555 1.34
LINK C LEU A 422 N MSE A 423 1555 1555 1.33
LINK C MSE A 423 N PHE A 424 1555 1555 1.32
LINK C ASP A 429 N MSE A 430 1555 1555 1.34
LINK C MSE A 430 N VAL A 431 1555 1555 1.34
LINK C ALA A 514 N MSE A 515 1555 1555 1.33
LINK C MSE A 515 N ASN A 516 1555 1555 1.32
LINK O GLU A 61 NA NA A 704 1555 1555 2.51
LINK O SER A 63 NA NA A 704 1555 1555 2.46
LINK O HOH A 637 NA NA A 704 1555 1555 2.29
LINK O HOH A 671 NA NA A 704 1555 1555 2.45
LINK NA NA A 704 O HOH A 751 1555 1555 2.66
LINK NA NA A 704 O HOH A1034 1555 1555 2.01
CISPEP 1 GLY A 372 THR A 373 0 8.77
CRYST1 114.272 114.272 83.723 90.00 90.00 120.00 P 32 2 1 6
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008751 0.005052 0.000000 0.00000
SCALE2 0.000000 0.010105 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011944 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
